scholarly journals Affinity Chromatography for Purification of IgG from Human Plasma

10.5772/36427 ◽  
2012 ◽  
Author(s):  
Lucia Hofbauer ◽  
Leopold Bruckschwaiger ◽  
Harald Arno ◽  
Wolfgang Teschner
Keyword(s):  
Affinity Chromatography ◽  
Human Plasma

Direct analysis – no sample preparation – of bioavailable cortisol in human plasma by weak affinity chromatography (WAC)

2017 ◽  
Vol 1061-1062 ◽  
pp. 438-444 ◽  
Author(s):  
Sten Ohlson ◽  
Jagjit Kaur ◽  
Manfred Raida ◽  
Ulf Niss ◽  
Tim Bengala ◽  
...  
Keyword(s):  
Sample Preparation ◽  
Affinity Chromatography ◽  
Human Plasma ◽  
Direct Analysis ◽  
No Sample Preparation

Purification of Corticosteroid-Binding Globulin from Human Plasma by Affinity Chromatography

1971 ◽  
Vol 33 (2) ◽  
pp. 193-198 ◽  
Author(s):  
WILLIAM ROSNER ◽  
H. LEON BRADLOW
Keyword(s):  
Affinity Chromatography ◽  
Human Plasma ◽  
Corticosteroid Binding Globulin

Distinction of Plasma Inhibitor of Activator-Induced Clot Lysis from Antiplasmins

1975 ◽  
Author(s):  
N. Aoki ◽  
M. Matsuda ◽  
M. Moroi ◽  
N. Yoshida
Keyword(s):  
Affinity Chromatography ◽  
Human Plasma ◽  
Gel Filtration ◽  
Plasminogen Activators ◽  
Inhibitory Effect ◽  
Clot Lysis ◽  
Plasminogen Activation ◽  
Lysis Time ◽  
Α2 Macroglobulin ◽  
Clot Lysis Time

A fraction of human plasma prolongs the activator-induced clot lysis time and inhibits plasminogen activation by the plasminogen activators derived from various sources (urine and tissues). This fraction, designated as antiactivator fraction, was separatid from antiplasmin fractions (α2-macroglobulin and α1-antitrypsin) by gel filtration and affinity chromatography on Sepharose coupled with IgG of antiserum to α1-antitrypsin. Anti-activator fraction thus obtained exerted little antiplasmin activity but inhibited strongly activator-induced clot lysis.Inhibitory effect of plasma on urokinase-induced clot lysis (antiactivator activity) was assayed in various diseases and compared with antiplasmin activity. No correlation was found between the two activities, and it was concluded that the two activities are independent and are ascribed to two different entities.

A Highly Purified Antithrombin III Concentrate Prepared From Human Plasma Fraction IV-1 by Affinity Chromatography

Vox Sanguinis ◽  
1994 ◽  
Vol 67 (2) ◽  
pp. 117-124 ◽  
Author(s):  
Wytold R. Lebing ◽  
David J. Hammond ◽  
James E. Wydick ◽  
George A. Baumbach
Keyword(s):  
Affinity Chromatography ◽  
Human Plasma ◽  
Antithrombin Iii ◽  
Plasma Fraction

Development of an improved fractionation of the human plasma proteome by a combination of abundant proteins depletion and multi-lectin affinity chromatography

Bioanalysis ◽  
2014 ◽  
Vol 6 (19) ◽  
pp. 2537-2548 ◽  
Author(s):  
Francisca O Gbormittah ◽  
Marina Hincapie ◽  
William S Hancock
Keyword(s):  
Affinity Chromatography ◽  
Human Plasma ◽  
Plasma Proteome ◽  
Lectin Affinity Chromatography ◽  
Lectin Affinity ◽  
Human Plasma Proteome

Purification of human plasma fibronectin using immobilized gelatin and Arg affinity chromatography

2008 ◽  
Vol 3 (3) ◽  
pp. 525-533 ◽  
Author(s):  
Pietro Speziale ◽  
Livia Visai ◽  
Simonetta Rindi ◽  
Antonella Di Poto
Keyword(s):  
Affinity Chromatography ◽  
Human Plasma ◽  
Plasma Fibronectin

Fibrinogen-Fibrin Interaction Studied by Affinity Chromatography

1975 ◽  
Author(s):  
A. Starnberger ◽  
H. Hörmann
Keyword(s):  
Affinity Chromatography ◽  
Human Plasma ◽  
Plasma Proteins ◽  
Plasma Fibrinogen ◽  
Covalently Linked ◽  
Deutsche Forschungsgemeinschaft

From human plasma, fibrinogen was adsorbed at 4° C on thrombin activated immobilized fibrinogen. Additionally retained plasma proteins were eluted at 37° C with 1.0 M Trisphosphate buffer, pH 7.6. Fibrinogen was subsequently eluted with 1.0 M KBr. It was free of contaminating proteins and showed a high clottability after removing KBr. Fibrin covalently linked to Sepharose 6B was reduced with dithioerythritol in 8 M urea. Washing with 8 M urea removed only औ-chains and γ-chains, while α-chains remained fixed to the insoluble matrix. Following carboxymethylation, the affinity of the immobilized α-chains to plasma fibrinogen was tested. Fibrinogen was adsorbed as described above. This may indicate that the α-chains are predominantly responsible for fibrinogen-fibrin interaction.Supported by the Deutsche Forschungsgemeinschaft, Sonderforschungsbereich 51.

Affinity chromatography of human plasma gelsolin with polyphosphate compounds on immobilized Cibacron Blue F3GA

1990 ◽  
Vol 526 ◽  
pp. 397-406 ◽  
Author(s):  
Hiroaki Ito ◽  
Hideo Yamamoto ◽  
Yoshihiro Kimura ◽  
Hiroshi Kambe ◽  
Toshikazu Okochi ◽  
...  
Keyword(s):  
Affinity Chromatography ◽  
Human Plasma ◽  
Cibacron Blue ◽  
Plasma Gelsolin ◽  
Cibacron Blue F3ga

[PHEMA/PEI]–Cu(II) based immobilized metal affinity chromatography cryogels: Application on the separation of IgG from human plasma

2016 ◽  
Vol 61 ◽  
pp. 824-831 ◽  
Author(s):  
Monireh Bakhshpour ◽  
Ali Derazshamshir ◽  
Nilay Bereli ◽  
Assem Elkak ◽  
Adil Denizli
Keyword(s):  
Affinity Chromatography ◽  
Human Plasma ◽  
Immobilized Metal Affinity Chromatography ◽  
Metal Affinity
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